60117-24-0

Basic information

• Product Name: LEU-ENKEPHALIN AMIDE
• Synonyms: enkephalinamide-leu;YGGFL-NH2;TYR-GLY-GLY-PHE-LEU-NH2;DYNORPHIN A (1-5) AMIDE;DYNORPHIN A (1-5) AMIDE ACETATE SALT;H-TYR-GLY-GLY-PHE-LEU-NH2;H-TYR-GLY-GLY-PHE-LEU-NH2 ACETATE SALT;LEU-ENKEPHALIN NH2
• CAS NO: 60117-24-0
• Molecular Formula: C₂₈H₃₈N₆O₆
• Molecular Weight: 554.64
• Mol File: 60117-24-0.mol
• Article Data: 20

Chemical Properties

• Melting Point: 123-126 °C
• Boiling Point: 1012.8 °C at 760 mmHg
• Flash Point: 566.3 °C
• Appearance: White powder
• Density: 1.254 g/cm³
• Vapor Pressure: 0mmHg at 25°C
• Refractive Index: 1.586
• Storage Temp.: −20°C
• PKA: 9.97±0.15(Predicted)
• CAS DataBase Reference: LEU-ENKEPHALIN AMIDE(CAS DataBase Reference)
• NIST Chemistry Reference: LEU-ENKEPHALIN AMIDE(60117-24-0)
• EPA Substance Registry System: LEU-ENKEPHALIN AMIDE(60117-24-0)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 60117-24-0(Hazardous Substances Data)

Usage

General Description

LEU-ENKEPHALIN AMIDE, also known as Leucine-enkephalin, is a pentapeptide that acts as an endogenous opioid neurotransmitter and has a role in pain regulation and stress response. It is derived from the precursor protein proenkephalin and is primarily found in the brain and adrenal medulla. Leu-enkephalin amide has been shown to have analgesic and antistress effects by binding to opioid receptors in the central nervous system, particularly the delta and mu opioid receptors. It is also involved in modulating mood, behavior, and the immune response. Research has suggested that leu-enkephalin amide may have therapeutic potential for managing pain and stress-related conditions.

InChI:InChI=1/C28H38N6O6/c1-17(2)12-22(26(30)38)34-28(40)23(14-18-6-4-3-5-7-18)33-25(37)16-31-24(36)15-32-27(39)21(29)13-19-8-10-20(35)11-9-19/h3-11,17,21-23,35H,12-16,29H2,1-2H3,(H2,30,38)(H,31,36)(H,32,39)(H,33,37)(H,34,40)

Upstream product

• 92176-50-6 N-Trt-Leucin-Enkephalinamid 
• 29022-11-5 N-(fluoren-9-ylmethoxycarbonyl)glycine 
• 35661-60-0 Fmoc-Leu-OH 
• 35661-40-6 N-Fmoc L-Phe 
• 71989-38-3 Fmoc-Tyr(tBu)-OH 
• 683218-30-6 N-(9-fluorenylmethyloxycarbonyl)-3-amino-3-(4,5-dimethoxy-2-nitrophenyl)propionic acid 
• 112883-29-1 N-Fmoc-Tyr-OH 
• 120-14-9 3,4-dimethoxy-benzaldehyde 
• 34840-85-2 3-amino-3-(3,4-dimethoxyphenyl)propanoic acid 
• 34841-03-7 methyl 3-amino-3-(3',4'-dimethoxyphenyl)propionate hydrochloride 
• 1445597-06-7 methyl 3-(3,4-dimethoxyphenyl)-3-(2,2,2-trifluoroacetamido)propanoate 
• 79396-89-7 Tyr-Gly-Gly-Phe-Leu-NH₂*HCOOH 
• 931114-55-5 α-Nsmoc-Gly-OH 
• 931114-58-8 α-Nsmoc-Leu-OH 

Downstream Products

• 71450-10-7 benzyl N-((1S)-2-[(1S)-1-(aminocarbonyl)-3-(methylsulfanyl)propyl]amino-1-benzyl-2-oxoethyl)carbamate 
• 71450-13-0 L-Phe-L-Met-NH₂ formate 
• 687-51-4 H-L-Leu-NH₂ 
• 60254-82-2 L-tyrosylglycylglycyl-L-phenylanine 

Relevant articles and documents

Environmentally friendly SPPS I. Application of NaOH in 2-MeTHF/methanol for Fmoc removal

Focusing on the step-by-step transformation of the traditional solid-phase peptide synthesis (SPPS) into an environmentally friendly process, we herein report the elimination of environmentally hazardous components (piperidine, DMF and DCM) from this technique. We developed a synthetic protocol that employs sodium hydroxide in a 2-MeTHF/MeOH mixture for Fmoc group cleavage and uses 2-MeTHF alone as the coupling solvent. The protocol was developed with the most frequently used PS/DVB-based resin. This synthetic strategy was used to prepare Leu-enkephalin amide, and the results (crude purity 99%, yield 62%) were fully comparable to those achieved with the traditional protocol using piperidine, DMF and DCM.

Core-shell-type resins for solid-phase peptide synthesis: Comparison with gel-type resins in solid-phase photolytic cleavage reaction

(Graph Presented) Novel core-shell-type resins with a rigid core and amino-functionalized flexible shell were prepared with 2,4,6-trichloro-1,3,5- triazine (CNC) and Jeffamine ED-600 starting from 1% cross-linked aminomethyl (AM) polystyrene resins. All o

Sustainable Peptide Synthesis Enabled by a Transient Protecting Group

The growing interest in synthetic peptides has prompted the development of viable methods for their sustainable production. Currently, large amounts of toxic solvents are required for peptide assembly from protected building blocks, and switching to water as a reaction medium remains a major hurdle in peptide chemistry. We report an aqueous solid-phase peptide synthesis strategy that is based on a water-compatible 2,7-disulfo-9-fluorenylmethoxycarbonyl (Smoc) protecting group. This approach enables peptide assembly under aqueous conditions, real-time monitoring of building block coupling, and efficient postsynthetic purification. The procedure for the synthesis of all natural and several non-natural Smoc-protected amino acids is described, as well as the assembly of 22 peptide sequences and the fundamental issues of SPPS, including the protecting group strategy, coupling and cleavage efficiency, stability under aqueous conditions, and crucial side reactions.

CITU: A Peptide and Decarboxylative Coupling Reagent

Tetrachloro-N-hydroxyphthalimide tetramethyluronium hexafluorophosphate (CITU) is disclosed as a convenient and economical reagent for both acylation and decarboxylative cross-coupling chemistries. Within the former set of reactions, CITU displays reactiv